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Volume 270, Number 33, Issue of August 18, pp. 19446-19450, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Formation of 2-Hydroxydeoxyadenosine Triphosphate, an Oxidatively Damaged Nucleotide, and Its Incorporation by DNA Polymerases
STEADY-STATE KINETICS OF THE INCORPORATION

(Received for publication, February 8, 1995; and in revised form, May 19, 1995)

Hiroyuki Kamiya ,  Hiroshi Kasai

We found that hydroxylation occurs at the C-2 position of adenine by oxygen radical treatment (Fe-EDTA) of dA, dATP, and single- and double-stranded DNA. This oxidatively damaged base, 2-hydroxyadenine, was produced 3-6-fold and 40-fold less than 8-hydroxyguanine when monomers and polynucleotides, respectively, were treated. To determine whether the damaged nucleotide, 2-hydroxydeoxyadenosine triphosphate (2-OH-dATP), is incorporated into a growing DNA, and to reveal the kinds of nucleotides opposite which 2-OH-dATP is incorporated, calf thymus DNA polymerase alpha and the Klenow fragment of Escherichia coli DNA polymerase I were used in in vitro DNA synthesis in the presence of 2-OH-dATP. DNA polymerase alpha incorporated the nucleotide opposite T and C in the DNA template. On the other hand, in an experiment using the Klenow fragment, incorporation of 2-OH-dATP was observed only opposite T. Steady-state kinetic studies indicated that incorporation of 2-OH-dATP by DNA polymerase alpha opposite T was favored over that opposite C by a factor of only 4.5. These results indicate that 2-OH-dATP, an oxidatively damaged nucleotide, is a substrate for DNA polymerases and is incorporated incorrectly by the replicative DNA polymerase.



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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.